Clues to how alpha-synuclein damages neurons in Parkinson's disease.
Identifieur interne : 001954 ( PubMed/Curation ); précédent : 001953; suivant : 001955Clues to how alpha-synuclein damages neurons in Parkinson's disease.
Auteurs : David Sulzer [États-Unis]Source :
- Movement disorders : official journal of the Movement Disorder Society [ 1531-8257 ] ; 2010.
English descriptors
- KwdEn :
- Humans, Inflammation (etiology), Lipids, Mutation (genetics), Neurons (cytology), Neurons (metabolism), Parkinson Disease (complications), Parkinson Disease (etiology), Parkinson Disease (genetics), Parkinson Disease (pathology), Secretory Vesicles (genetics), Secretory Vesicles (metabolism), Secretory Vesicles (pathology), alpha-Synuclein (genetics), alpha-Synuclein (metabolism).
- MESH :
- chemical , genetics : alpha-Synuclein.
- chemical , metabolism : alpha-Synuclein.
- chemical : Lipids.
- complications : Parkinson Disease.
- cytology : Neurons.
- etiology : Inflammation, Parkinson Disease.
- genetics : Mutation, Parkinson Disease, Secretory Vesicles.
- metabolism : Neurons, Secretory Vesicles.
- pathology : Parkinson Disease, Secretory Vesicles.
- Humans.
Abstract
Alpha-synuclein (alpha-syn) appears to normally regulate neurotransmitter release, possibly via calcium-dependent binding and dissociation from lipid domains on secretory vesicles. The pathogenic effects of alpha-syn leading to Parkinson's disease (PD) appear to result from alternate toxic effects on lipid membrane. A variety of findings indicate that overexpression of wild-type alpha-syn, pathogenic mutations of alpha-syn, and dopamine-modified-alpha-syn promote toxic interaction between alpha-syn oligomers and lipids. These may disrupt transmembrane concentration gradients across secretory vesicles and other organelles and interfere with normal lysosomal or ubiqutin/proteasome mediated protein degradation or mitochondrial function. Additional causes of PD may interfere at other points with normal handling and degradation of alpha-syn, providing a variety of entry points to a converging neurodegenerative path underlying the disease.
DOI: 10.1002/mds.22639
PubMed: 20187229
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The pathogenic effects of alpha-syn leading to Parkinson's disease (PD) appear to result from alternate toxic effects on lipid membrane. A variety of findings indicate that overexpression of wild-type alpha-syn, pathogenic mutations of alpha-syn, and dopamine-modified-alpha-syn promote toxic interaction between alpha-syn oligomers and lipids. These may disrupt transmembrane concentration gradients across secretory vesicles and other organelles and interfere with normal lysosomal or ubiqutin/proteasome mediated protein degradation or mitochondrial function. Additional causes of PD may interfere at other points with normal handling and degradation of alpha-syn, providing a variety of entry points to a converging neurodegenerative path underlying the disease.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">20187229</PMID><DateCreated><Year>2010</Year><Month>03</Month><Day>03</Day></DateCreated><DateCompleted><Year>2010</Year><Month>06</Month><Day>14</Day></DateCompleted><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1531-8257</ISSN><JournalIssue CitedMedium="Internet"><Volume>25 Suppl 1</Volume><PubDate><Year>2010</Year></PubDate></JournalIssue><Title>Movement disorders : official journal of the Movement Disorder Society</Title><ISOAbbreviation>Mov. 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These may disrupt transmembrane concentration gradients across secretory vesicles and other organelles and interfere with normal lysosomal or ubiqutin/proteasome mediated protein degradation or mitochondrial function. 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